What is the Difference Between Enzyme Activator and Enzyme Inhibitor?
🆚 Go to Comparative Table 🆚Enzyme activators and enzyme inhibitors are two types of molecules that can affect the activity of an enzyme. The main difference between them is their impact on enzyme function:
- Enzyme Activator: These molecules increase the activity of an enzyme, thereby enhancing its catalytic ability. They can bind to locations on an enzyme other than the active site, causing an increase in the function of the active site. Some enzyme activators also facilitate allosteric regulation, where the binding of an activator at one site on the enzyme can lead to the creation of more profitable conformers that can accelerate the enzymatic reaction.
- Enzyme Inhibitor: These molecules decrease the activity of an enzyme by binding to it and preventing it from catalyzing reactions. Inhibitors can be classified into two main types: competitive and noncompetitive inhibitors. Competitive inhibitors bind the enzyme at its active site, blocking the binding of the substrate and competing with it for the enzyme's attention. Noncompetitive inhibitors, on the other hand, bind to other parts of the enzyme, changing its structure and reducing its activity.
In summary, enzyme activators enhance enzyme function, while enzyme inhibitors reduce it. Both activators and inhibitors play crucial roles in regulating enzyme activity and can be found in various biological and pharmacological contexts.
On this pageWhat is the Difference Between Enzyme Activator and Enzyme Inhibitor? Comparative Table: Enzyme Activator vs Enzyme Inhibitor
Comparative Table: Enzyme Activator vs Enzyme Inhibitor
Here is a table comparing enzyme activators and enzyme inhibitors:
Enzyme Activators | Enzyme Inhibitors |
---|---|
Chemical species that bind with an enzyme to increase its activity | Chemical species that bind with an enzyme to decrease its activity |
Act by binding to allosteric sites of the enzyme, not the active site | Bind to the active site of the enzyme, preventing substrate binding |
Increase the rate of enzymatic reactions | Decrease the rate of enzymatic reactions |
Examples include hexokinase-I and glucokinase | Examples include drugs and ribonuclease inhibitor |
In summary, enzyme activators increase the activity of an enzyme by binding to allosteric sites, while enzyme inhibitors decrease the activity of an enzyme by binding to the active site, preventing substrate binding.
Read more:
- Enzyme Inhibitor vs Enzyme Inducer
- Catalyst vs Inhibitor
- Catalyst vs Enzyme
- Enzyme Activity vs Specific Activity
- Enzyme vs Coenzyme
- Metalloenzymes vs Metal Activated Enzymes
- Cell Immobilization vs Enzyme Immobilization
- Enzyme vs Protein
- Enzyme vs Hormone
- Activator Promoter vs Repressor
- Free vs Immobilized Enzymes
- Anabolic vs Catabolic Enzymes
- Isomerase vs Mutase Enzyme
- Proteolytic Enzymes vs Digestive Enzymes
- Allosteric vs Non-allosteric Enzymes
- Acid Hydrolysis vs Enzymatic Hydrolysis
- Enzymatic vs Nonenzymatic Reaction
- Exoenzyme vs Endoenzyme
- Intracellular vs Extracellular Enzymes